Efficient construction of a large nonimmune phage antibody library: The production of high-affinity human single-chain antibodies to protein antigens

Abstract

authors request that the following corrections be noted. It was accidentally stated that the studies by Kajita et al. (1) and Lee et al. (2) dealt with cinnamoyl-CoA reductase modified plants when in fact they concerned 4-coumarate:coenzyme A ligase (4CL) transgenic plants. Lignin concentration was reduced by down-regulation of 4CL activity in both studies (1, 2). In a subsequent article, Kajita et al. (3) reported a negligible decrease in lignin concentration and a decreased syringyl-toguaiacyl ratio for lignin composition of a sense-suppressed 4CL transgenic tobacco line. Kajita et al. (1) rather than Kajita et al. (3) was inadvertently cited when this later report was contrasted with the large decreases in lignin concentration and an increased syringyl-to-guaiacyl lignin ratio for anti-sense suppressed 4CL Arabidopsis transgenics (2). The authors apologize for the confusion these errors have created for readers of their Commentary and to the authors of the cited work for misrepresenting their research. November 10, 1998, of Proc. Natl. Acad. Sci. USA (95, 13612-13617), the authors request that the following correction be noted: In Fig. 2 appearing on page 13614, the genotype identification for testicular histology in panels C and D were shown reversed. The correct identification is Ϫ͞Ϫ for panel C and ϩ͞ϩ for panel D. The fifth sentence of the figure legend should read as follows: "Histological sections at lower (E) and higher (D) magnification of the seminiferous tubuli from a wild-type and mutant (F and C) mouse."Cell Biology. In the article "Efficient construction of a large nonimmune phage antibody library: The production of highaffinity human single-chain antibodies to protein antigens" by

Selecting Open Reading Frames From DNA

“…gene represented by 1000 different clones) when compared with the sizes of phage antibody libraries that have been made by standard cloning methods (10 9-10 ; Vaughan et al 1996;Sheets et al 1998). The application of this technology to fragmented pathogenic organisms will permit the selection of antigenic epitopes recognized by patient sera, as has already been carried out using random peptide libraries (Cortese et al 1994(Cortese et al , 1995(Cortese et al , 1996, with the possibility of identifying highly antigenic regions suitable as protein or DNA vaccines.…”

A visible phagemid system for the estimation of Cre-mediated recombination efficiency

“…It is difficult to obtain an antibody library size over 1 Â 10 10 using traditional phage display whereby antibody diversity is created by random combinatorial linkage of V H and V L genes and cloning, due to the limited efficiency of bacterial transformation (10 9 cfu/ml). Evidence showing that a larger initial phage antibody library results in significantly higher possibility of selection for high-affinity antigen-specific antibodies has encouraged further attempts to increase initial antibody library sizes (Vaughan et al, 1996;Sheets et al, 1998;Knappik et al, 2000).…”

A library of bacteriophage-displayed antibody fragments directed against proteins of the inner ear

“…Although prior immunization enhances the probability of acquiring immunological reagents that recognize a particular antigen, the absolute requirement for an immune response is obviated by the generation during library construction of antibody fragments that are not expressed in vivo and that recognize new epitopes (13). This feature should permit the isolation of immunological reagents when minimal antigen is available for immunization, when it is necessary to immunize with a heterogenous complex of proteins, when proteins are highly conserved between species, or when antibodies must be isolated against uncharacterized proteins.…”